EXPRESSION IN ESCHERICHIA-COLI AND PHOSPHORYLATION WITH CAMP-DEPENDENT PROTEIN-KINASE OF THE N-TERMINAL REGION OF HUMAN ENDOTHELIAL ACTIN-BINDING PROTEIN

The N-terminal region of human endothelial actin-binding protein was s ubcloned and expressed in the pT 7-7/E. coli BL 21 (DE 3) system. This peptide was efficiently expressed in E. coli as indicated by sodium d odecyl sulfate-polyacrylamide gel electrophoresis and by western analy sis using a monoclonal antibody raised against this part of the molecu le. As predicted by the amino acid sequence this truncated protein (re sidues 21-1569), corresponding to 164 KD and containing the actin-bind ing domain near the amino-terminus, could be phosphorylated by cAMP-de pendent protein kinase unmasking a phosphorylation site which is not a pparent in the native ABP protein. (C) 1994 Academic Press, Inc.